ID A0A0F7N7Y2_9ACTN Unreviewed; 674 AA.
AC A0A0F7N7Y2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Molybdopterin molybdenumtransferase {ECO:0000256|RuleBase:RU365090};
DE EC=2.10.1.1 {ECO:0000256|RuleBase:RU365090};
GN ORFNames=AA958_16475 {ECO:0000313|EMBL:AKH83538.1};
OS Streptomyces sp. CNQ-509.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH83538.1, ECO:0000313|Proteomes:UP000034283};
RN [1] {ECO:0000313|EMBL:AKH83538.1, ECO:0000313|Proteomes:UP000034283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH83538.1,
RC ECO:0000313|Proteomes:UP000034283};
RA Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA Kalinowski J., Heide L., Kaysser L.;
RT "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific Producer
RT of Meroterpenoid Chemistry.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the insertion of molybdate into adenylated
CC molybdopterin with the concomitant release of AMP.
CC {ECO:0000256|ARBA:ARBA00002901, ECO:0000256|RuleBase:RU365090}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-
CC molybdopterin; Xref=Rhea:RHEA:35047, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36264, ChEBI:CHEBI:62727,
CC ChEBI:CHEBI:71302, ChEBI:CHEBI:456215; EC=2.10.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001529};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU365090};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046, ECO:0000256|RuleBase:RU365090}.
CC -!- SIMILARITY: Belongs to the MoeA family. {ECO:0000256|ARBA:ARBA00010763,
CC ECO:0000256|RuleBase:RU365090}.
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DR EMBL; CP011492; AKH83538.1; -; Genomic_DNA.
DR RefSeq; WP_047016843.1; NZ_CP011492.1.
DR AlphaFoldDB; A0A0F7N7Y2; -.
DR STRING; 444103.AA958_16475; -.
DR KEGG; strc:AA958_16475; -.
DR PATRIC; fig|444103.5.peg.3467; -.
DR OrthoDB; 3196725at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000034283; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00887; MoeA; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR Gene3D; 2.40.340.10; MoeA, C-terminal, domain IV; 1.
DR Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR Gene3D; 2.170.190.11; Molybdopterin biosynthesis moea protein, domain 3; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR038987; MoeA-like.
DR InterPro; IPR005111; MoeA_C_domain_IV.
DR InterPro; IPR036688; MoeA_C_domain_IV_sf.
DR InterPro; IPR005110; MoeA_linker/N.
DR InterPro; IPR036135; MoeA_linker/N_sf.
DR PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF03454; MoeA_C; 1.
DR Pfam; PF03453; MoeA_N; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF63882; MoeA N-terminal region -like; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|RuleBase:RU365090};
KW Metal-binding {ECO:0000256|RuleBase:RU365090};
KW Molybdenum {ECO:0000256|RuleBase:RU365090};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|RuleBase:RU365090};
KW Reference proteome {ECO:0000313|Proteomes:UP000034283};
KW Transferase {ECO:0000256|RuleBase:RU365090}.
FT DOMAIN 391..527
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 674 AA; 67621 MW; 5D81DAA82F9FA5F3 CRC64;
MTSGRRGERR TPGAGAGGGS GNGSDGETGA RGDEFADALA LANDRRDLAA AYGDAFTLAD
PPPPEAPAGR VRPGTSREGA RTDEFGDALA FTDRNGTEGA AARGAGARAD RGARGRGDAF
AAPSARTGPG PRAEGRSSGR GARDGSDRDP RERAGGSAPT PPRTGPGRRP DGRAGSDGAG
APAARTGSGR GGDPLDVALG LAGRARREPG DPRGLSWDAA RRVAVRSGRR LGAVAVPVAG
AYGQVLAEPL RALADLPPFD TSAMDGYAVA GPGPWRLDAS GQGILAGHAA HPALPDGHAV
RIATGARVPP GATGVLRSEH AELRDDGSLY ATGATAAQDV RTGQDIRPRG QECRAGAELL
PAGARVTPAV LGLAAAAGHD ELRVVRSPRV EILVLGAELL HRGLPREGRI RDALGPMLEP
WLRACGAEPF VTRRLGDDAE LLYEAVATST ADVVVTTGGT AAGPVDHVHG TLRRLKADLV
VDGVAVRPGH PMLLAVLPTG AHVVGLPGNP LAAVSGLLTL AEPLVRVLGG APVPESPEAV
LIADVKGHPT DTRLVPVALE HGAHAPAAHR PARTERPAPT APAAQIPPPG AQRPARTPAG
GAHAAPVRAA ASGAPYPAAR PLHFTGPAML RGLAVADALA VVPPGGAPAG TPVRVLRLPW
AAAPPAATTP AGPA
//